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LINK . SPRINGER . COM {}

  1. Analyzed Page
  2. Matching Content Categories
  3. CMS
  4. Monthly Traffic Estimate
  5. How Does Link.springer.com Make Money
  6. Keywords
  7. Topics
  8. Questions
  9. Schema
  10. External Links
  11. Analytics And Tracking
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We are analyzing https://link.springer.com/chapter/10.1007/978-3-319-20149-8_12.

Title:
Perforins | SpringerLink
Description:
“Perforins” – cytotoxic cell perforin-1, proteins contributing to the complement membrane attack complex (MAC) and other perforin-like proteins – form unconventional pores in biological membranes in the sense that as well as a ring of subunits...
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {πŸ“š}

  • Education
  • Business & Finance
  • Telecommunications

Content Management System {πŸ“}

What CMS is link.springer.com built with?

Custom-built

No common CMS systems were detected on Link.springer.com, and no known web development framework was identified.

Traffic Estimate {πŸ“ˆ}

What is the average monthly size of link.springer.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month


Based on our best estimate, this website will receive around 5,000,019 visitors per month in the current month.
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How Does Link.springer.com Make Money? {πŸ’Έ}

We don’t know how the website earns money.

Not all websites focus on profit; some are designed to educate, connect people, or share useful tools. People create websites for numerous reasons. And this could be one such example. Link.springer.com could be getting rich in stealth mode, or the way it's monetizing isn't detectable.

Keywords {πŸ”}

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Topics {βœ’οΈ}

month download article/chapter garcia-saez aj perforin-mediated target-cell death phospholipid-binding c2 domain myd88-dependent signaling pathway form widely-varying sizes beta-sheet transition identified resulting arc-pore structures membrane attack complex/perforin glial-guided neuronal migration binary pore-forming proteins bax central helices perforin-mediated myocardial damage cytolytic pore-forming protein cell-membrane pores induced c8alpha-macpf reveals mechanism purified pore-forming protein ion channel-forming properties bacterial toxin pneumolysin bacterial cholesterol-dependent cytolysin cytotoxic t-cell granules perforin-related protein pleurotolysin facilitate rapid access plasma membrane repair pore-forming toxin privacy choices/manage cookies membrane attack complex conductance fluctuations induced device instant download eukaryotic protein toxin editor information editors persechini pm induce cell death regulate drosophila growth ojcius dm pore-forming toxins pore-forming protein sonnen af macpf/cdc family shepard la pore-forming proteins macpf/cdc proteins cytolytic pore lined killer cell attack calcium-dependent permeabilization peptide-induced pores rapid membrane disruption membrane-spanning domain endosomal membrane trigger mitochondrial outer membrane

Questions {❓}

  • Teissie J, Golzio M, Rols MP (2005) Mechanisms of cell membrane electropermeabilization: a minireview of our present (lack of ?

Schema {πŸ—ΊοΈ}

ScholarlyArticle:
      headline:Perforins
      pageEnd:312
      pageStart:289
      image:https://media.springernature.com/w153/springer-static/cover/book/978-3-319-20149-8.jpg
      genre:
         Biomedical and Life Sciences
         Biomedical and Life Sciences (R0)
      isPartOf:
         name:Electrophysiology of Unconventional Channels and Pores
         isbn:
            978-3-319-20149-8
            978-3-319-20148-1
         type:Book
      publisher:
         name:Springer International Publishing
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Robert J. C. Gilbert
            affiliation:
                  name:Wellcome Trust Centre for Human Genetics, University of Oxford
                  address:
                     name:Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      keywords:Perforin, Complement membrane attack complex, Toroidal pore, Proteolipidic pore, Single channel conductance
      description:β€œPerforins” – cytotoxic cell perforin-1, proteins contributing to the complement membrane attack complex (MAC) and other perforin-like proteins – form unconventional pores in biological membranes in the sense that as well as a ring of subunits circumscribing an opening in the lipid bilayer, arcs of subunits induce similar effects. The resulting arc-pore structures are completed by a lipidic edge, conferring distinctive functional characteristics on them. Electrophysiological measurements have played a distinguished role in the discovery and characterisation of this alternative mechanism of pore formation which enables the same protein to form widely-varying sizes of pore and enact a greater diversity of effects than more conventional channels. This review discusses the mechanism of pore formation by the perforins and the way in which it has been illuminated by electrical conductance studies alongside imaging methods such as electron microscopy and atomic force microscopy.
      datePublished:2015
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
      context:https://schema.org
Book:
      name:Electrophysiology of Unconventional Channels and Pores
      isbn:
         978-3-319-20149-8
         978-3-319-20148-1
Organization:
      name:Springer International Publishing
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Wellcome Trust Centre for Human Genetics, University of Oxford
      address:
         name:Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Robert J. C. Gilbert
      affiliation:
            name:Wellcome Trust Centre for Human Genetics, University of Oxford
            address:
               name:Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {πŸ”—}(334)

Analytics and Tracking {πŸ“Š}

  • Google Tag Manager

Libraries {πŸ“š}

  • Clipboard.js

CDN Services {πŸ“¦}

  • Pbgrd

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